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2CHA

THE STRUCTURE OF CRYSTALLINE ALPHA-CHYMOTRYPSIN, $V.THE ATOMIC STRUCTURE OF TOSYL-ALPHA-CHYMOTRYPSIN AT 2 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
C0004252molecular_functionserine-type endopeptidase activity
C0006508biological_processproteolysis
F0004252molecular_functionserine-type endopeptidase activity
F0006508biological_processproteolysis
G0004252molecular_functionserine-type endopeptidase activity
G0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TSU C 51
ChainResidue
BHIS57
CSER190
CCYS191
CMET192
CGLY193
CASP194
CSER195
CGLY216
FTYR146

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TSU G 51
ChainResidue
BTYR146
FHIS57
GSER190
GCYS191
GMET192
GGLY193
GASP194
GSER195
GGLY216

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC
ChainResidueDetails
BVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. SScmGDSGGPLV
ChainResidueDetails
CSER189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Charge relay system
ChainResidueDetails
CSER195
GSER195
FHIS57
FASP102

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 387
ChainResidueDetails
CGLY193electrostatic stabiliser
CSER195covalent catalysis
CGLY196electrostatic stabiliser

site_idMCSA2
Number of Residues3
DetailsM-CSA 387
ChainResidueDetails
GGLY193electrostatic stabiliser
GSER195covalent catalysis
GGLY196electrostatic stabiliser

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PDB entries from 2024-04-24

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